Abstract: Novel elgin mutants that differ from the natural eglins B and C by the replacement of one, two or three amino acids in the region of the active center (amino acids 45 and 46, Leu-Asp) by other amino acids are provided. The mutants, which can be produced by recombinant genetic engineering, have valuable pharmacological properties.

Abstract: The invention relates to synthetic peptides which have amino acid sequences which correspond, in whole or in part, to the amino acid sequence of prothrombin and are antigenic, to the use thereof for the immunization of an animal and for the purification of specific antibodies, to antibodies against these peptides, and to the use of the antibodies for the determination of the fragments F.sub.2 /F.sub.1+2.

Abstract: The present invention relates to genes and their encoded proteins which induce immunological effector cell activation and chemattraction. The proteins of the invention attract subsets of immunological effector cells and stimulate them to express their specialized effector cell functions. Such proteins, termed Ap-1 proteins, are expressed by lymphoid cells, and bind to effector cells such as macrophages and mast cells. In particular, the Ap-1 proteins induce macrophage phagocytosis, expression of class II major histocompatibility molecules, cytotoxicity, and migration, and induce hematopoietic progenitor cell differentiation. The Ap-1 molecules can be of value in the therapy or diagnosis of inflammatory or immune disorders, or neoplasia.

Abstract: Mammalian melanin-concentrating hormone (MCH) is isolated from rat tissue, purified and characterized. These MCH peptides are useful for treating skin disorders, for suppressing the proliferation of skin tumor cells, such as melanomas in mammals, and for modulating the secretion of ACTH. Generally, peptides are provided which have the following formula: ##STR1## or which are naturally occurring homologs of the peptide with said formula. The peptides which are the naturally occurring MCH homologs of mammalian species other than rat can also be obtained using the materials disclosed, as demonstrated specifically with human MCH, which is found to have the same structure as rat MCH. Also disclosed are the amino acid sequences of, and the nucleotide sequences of the cDNAs which encode, the putative precursors of rat MCH and human MCH. These precursors may also include one or more biologically active peptides N-terminally of the mature MCH's.

Abstract: This invention provides a purified polypeptide useful as an antimicrobial agent. This purified polypeptide has been derived from human granulocytes, and has a molecular weight of about 3,700 daltons and the N-terminal amino acid sequence val-cys-ser-cys-arg-leu-val-phe-cys-arg-arg-thr-glu- leu-arg-val-gly-asn-cys-leu-ile-gly-gly-val-ser-phe-thr-try-cys-thr-arg-va l. This invention also provides methods for producing this polypeptide, pharmaceutical compositions containing the polypeptide, and uses thereof.

Abstract: A novel physiologically active polypeptide having antitumor activity obtained by improving human tumor necrosis factor (TNF). The amino acid sequence of the polypeptide essentially corresponds to that of human tumor necrosis factor, except that ten amino acids Nos. 1 to 10 are deleted and (Met).sub.n -Arg-Lys-Arg are added to the amino (NH.sub.2)-terminus, where n is 0 or 1. Other amino acid modifications can also be made to the polypeptide while retaining high antitumor activity. The novel polypeptide has less side effects that the natural-type TNF, particularly with respect to cytotoxicity. A a DNA fragment encoding the polypeptide, a recombinant plasmid containing the DNA fragment, a recombinant microorganism cell transformed with the plasmid, a method of producing a novel physiologically active polypeptide using the microorganism cell, and a pharmaceutical composition comprising the polypeptide as an active ingredient are also provided.

Abstract: An isolated DNA sequence encoding an angiogenic factor protein consisting of a single-polypeptide-chain protein having at least one active site possessing mitotic and chemotactic activity and the ability to stimulate protease synthesis, wherein said protein consists of the amino acid sequence: ##STR1## In a preferred embodiment, the DNA sequence encodes basic fibroblast growth factor (bFGF).

Abstract: Genes and DNA transfer vectors for the expression of human preprorelaxin; sub-units thereof, including genes and transfer vectors for expression of human prorelaxin and the individual A, B and C peptide chains thereof; and equivalents of all such genes. Methods for synthesis of the peptides involving recombinant DNA techniques.

Abstract: An angiogenic factor is disclosed which is a purified, single-polypeptide-chain protein having at least one active site possessing an activity selected from the group consisting of mitogenic activity, chemotactic activity, the ability to stimulate protease synthesis and combinations thereof. This angiogenic factor exhibits substantial homology to and is immunologically equivalent to the native angiogenic factor isolatable from human placental tissues. The amino acid sequence of this angiogenic factor is also disclosed. In addition, a method for isolation of the purified angiogenic factor from human placental tissues is set forth. Pharmaceutical preparations incorporating this angiogenic factor are described.

Abstract: There is disclosed an isolated DNA sequence and the amino acid sequence for human factor IX. The isolated DNA sequence and its flanking sequences are useful for determining mutations, deletions or other modifications in genetic sequences expressing normal factor IX or modifications thereof.

Abstract: A recombinant subunit vaccine for protecting dogs against infection caused by canine parvovirus comprising VP-2 protein produced during replication of a recombinant baculovirus in insect tissue culture cells or insects which are a permissive host for the replication of selected baculoviruses.

Abstract: DNA sequences, recombinant DNA molecules and hosts transformed with them which produce human lipocortin-like polypeptides and methods of making and using these products. The DNA sequences and recombinant DNA molecules are characterized in that they code on expression for a human lipocortin-like polypeptide. In appropriate hosts these DNA sequences permit the production of human lipocortin-like polypeptides useful as anti-inflammatory agents and methods in the treatment of arthritic, allergic, dermatologic, ophthalmic and collagen diseases as well as other disorders involving inflammatory processes.